脂肪酸从脂肪酸结合蛋白释放的一种可能途径。
A possible route for the release of fatty acid from fatty acid-binding protein.
作者信息
Zanotti G, Feltre L, Spadon P
机构信息
Department of Organic Chemistry, Padova University, Italy.
出版信息
Biochem J. 1994 Jul 15;301 ( Pt 2)(Pt 2):459-63. doi: 10.1042/bj3010459.
A simulation of the release of fatty acid from intestinal fatty acid-binding protein was attempted, starting with the crystallographic model and using molecular-dynamic processes at different temperatures. The release of the ligand was observed only at high temperature, which perhaps makes the process unreliable in detail. Nevertheless, the overall behaviour of the protein, also confirmed by the simulation performed at room temperature, strongly supports the idea that the fatty acid leaves the protein through an opening formed by alpha-helix II and turns beta C-beta D and beta E-beta F. Additionally, it suggests a role for the lack of hydrogen bonds between the main chains of beta-strands D and E: this feature, observed in all the protein structures of this family which have currently been determined, seems to provide the structure with great flexibility, allowing the barrel to open and close without disruption of the hydrogen-bond network.
从晶体学模型出发，利用不同温度下的分子动力学过程，尝试对肠道脂肪酸结合蛋白中脂肪酸的释放进行模拟。仅在高温下观察到配体的释放，这可能使该过程在细节上不可靠。然而，该蛋白的整体行为，在室温下进行的模拟也得到了证实，有力地支持了脂肪酸通过由α-螺旋II以及β链C-β链D和β链E-β链F形成的开口离开蛋白的观点。此外，这表明β链D和E主链之间缺乏氢键具有一定作用：在目前已确定的该家族所有蛋白质结构中都观察到这一特征，它似乎赋予结构很大的灵活性，使桶状结构能够打开和关闭而不破坏氢键网络。
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